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P99024

- TBB5_MOUSE

UniProt

P99024 - TBB5_MOUSE

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Protein

Tubulin beta-5 chain

Gene

Tubb5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB
  3. structural constituent of cytoskeleton Source: MGI

GO - Biological processi

  1. microtubule-based process Source: UniProtKB
  2. protein folding Source: Reactome
  3. protein polymerization Source: InterPro
  4. spindle assembly Source: MGI
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-5 chain
Gene namesi
Name:Tubb5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:107812. Tubb5.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. microtubule Source: MGI
  5. nuclear envelope lumen Source: Ensembl
  6. nucleus Source: MGI
  7. tubulin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Disruption phenotypei

Results in a perturbation of the cell cycle of neurogenic progenitors as well as an alteration in the position of migrating neurons. There is a decrease in neurons in the cortical plate and an accumulation of cells within the ventricular and intermediate zones.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Tubulin beta-5 chainPRO_0000048246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581N6-acetyllysine; alternate1 Publication
Modified residuei58 – 581N6-succinyllysine; alternate1 Publication
Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity
Modified residuei318 – 3181Omega-N-methylarginineBy similarity
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP99024.
PRIDEiP99024.

2D gel databases

REPRODUCTION-2DPAGEIPI00117352.
P99024.
SWISS-2DPAGEP99024.

PTM databases

PhosphoSiteiP99024.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in spleen, thymus and immature brain. Expressed in embryonic brain, including throughout the developing cortex and in the subventricular zone. Also found in radial glial cells, intermediate progenitors, migrating neurons and postmitotic neurons.1 Publication

Gene expression databases

BgeeiP99024.
CleanExiMM_TUBB5.
ExpressionAtlasiP99024. baseline and differential.
GenevestigatoriP99024.

Interactioni

Subunit structurei

Interacts with MX1 By similarity. Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO. May interact with RNABP10.By similarity2 Publications

Protein-protein interaction databases

BioGridi204381. 30 interactions.
IntActiP99024. 32 interactions.
MINTiMINT-1869561.

Structurei

3D structure databases

ProteinModelPortaliP99024.
SMRiP99024. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119061.
HOVERGENiHBG000089.
InParanoidiP99024.
KOiK07375.
OMAiTPPPHIF.
OrthoDBiEOG71ZP1H.
PhylomeDBiP99024.
TreeFamiTF300298.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P99024-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY
60 70 80 90 100
YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA
Length:444
Mass (Da):49,671
Last modified:August 13, 1987 - v1
Checksum:i1E6CD0A36773A103
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Q → P in BAB27292. (PubMed:16141072)Curated
Sequence conflicti114 – 1141D → N in BAE40217. (PubMed:16141072)Curated
Sequence conflicti143 – 1431T → N in BAE28709. (PubMed:16141072)Curated
Sequence conflicti264 – 2641H → D in BAE40217. (PubMed:16141072)Curated
Sequence conflicti307 – 3071H → N in BAE39835. (PubMed:16141072)Curated
Sequence conflicti357 – 3571P → T in BAE40217. (PubMed:16141072)Curated
Sequence conflicti400 – 4001G → A in AAA40510. (PubMed:3839797)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04663 mRNA. Translation: CAA28369.1.
AK010960 mRNA. Translation: BAB27292.1.
AK011263 mRNA. Translation: BAB27504.1.
AK051164 mRNA. Translation: BAC34541.1.
AK051393 mRNA. Translation: BAC34623.1.
AK083327 mRNA. Translation: BAC38866.1.
AK146567 mRNA. Translation: BAE27265.1.
AK148978 mRNA. Translation: BAE28709.1.
AK151215 mRNA. Translation: BAE30210.1.
AK151670 mRNA. Translation: BAE30596.1.
AK160225 mRNA. Translation: BAE35700.1.
AK161575 mRNA. Translation: BAE36471.1.
AK165249 mRNA. Translation: BAE38103.1.
AK167691 mRNA. Translation: BAE39738.1.
AK167779 mRNA. Translation: BAE39811.1.
AK167808 mRNA. Translation: BAE39835.1.
AK167926 mRNA. Translation: BAE39931.1.
AK168271 mRNA. Translation: BAE40217.1.
AK169123 mRNA. Translation: BAE40903.1.
AK169210 mRNA. Translation: BAE40982.1.
AK169295 mRNA. Translation: BAE41051.1.
CR974451 Genomic DNA. Translation: CAO77890.1.
BC003825 mRNA. Translation: AAH03825.1.
M28732 mRNA. Translation: AAA40510.1.
CCDSiCCDS28706.1.
PIRiE25437.
RefSeqiNP_035785.1. NM_011655.5.
UniGeneiMm.273538.
Mm.472638.

Genome annotation databases

EnsembliENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
GeneIDi22154.
KEGGimmu:22154.
UCSCiuc008ciq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04663 mRNA. Translation: CAA28369.1 .
AK010960 mRNA. Translation: BAB27292.1 .
AK011263 mRNA. Translation: BAB27504.1 .
AK051164 mRNA. Translation: BAC34541.1 .
AK051393 mRNA. Translation: BAC34623.1 .
AK083327 mRNA. Translation: BAC38866.1 .
AK146567 mRNA. Translation: BAE27265.1 .
AK148978 mRNA. Translation: BAE28709.1 .
AK151215 mRNA. Translation: BAE30210.1 .
AK151670 mRNA. Translation: BAE30596.1 .
AK160225 mRNA. Translation: BAE35700.1 .
AK161575 mRNA. Translation: BAE36471.1 .
AK165249 mRNA. Translation: BAE38103.1 .
AK167691 mRNA. Translation: BAE39738.1 .
AK167779 mRNA. Translation: BAE39811.1 .
AK167808 mRNA. Translation: BAE39835.1 .
AK167926 mRNA. Translation: BAE39931.1 .
AK168271 mRNA. Translation: BAE40217.1 .
AK169123 mRNA. Translation: BAE40903.1 .
AK169210 mRNA. Translation: BAE40982.1 .
AK169295 mRNA. Translation: BAE41051.1 .
CR974451 Genomic DNA. Translation: CAO77890.1 .
BC003825 mRNA. Translation: AAH03825.1 .
M28732 mRNA. Translation: AAA40510.1 .
CCDSi CCDS28706.1.
PIRi E25437.
RefSeqi NP_035785.1. NM_011655.5.
UniGenei Mm.273538.
Mm.472638.

3D structure databases

ProteinModelPortali P99024.
SMRi P99024. Positions 2-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204381. 30 interactions.
IntActi P99024. 32 interactions.
MINTi MINT-1869561.

Chemistry

BindingDBi P99024.

PTM databases

PhosphoSitei P99024.

2D gel databases

REPRODUCTION-2DPAGE IPI00117352.
P99024.
SWISS-2DPAGE P99024.

Proteomic databases

MaxQBi P99024.
PRIDEi P99024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001566 ; ENSMUSP00000001566 ; ENSMUSG00000001525 .
GeneIDi 22154.
KEGGi mmu:22154.
UCSCi uc008ciq.2. mouse.

Organism-specific databases

CTDi 22154.
MGIi MGI:107812. Tubb5.

Phylogenomic databases

GeneTreei ENSGT00760000119061.
HOVERGENi HBG000089.
InParanoidi P99024.
KOi K07375.
OMAi TPPPHIF.
OrthoDBi EOG71ZP1H.
PhylomeDBi P99024.
TreeFami TF300298.

Enzyme and pathway databases

Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSi TUBB. mouse.
NextBioi 302074.
PROi P99024.
SOURCEi Search...

Gene expression databases

Bgeei P99024.
CleanExi MM_TUBB5.
ExpressionAtlasi P99024. baseline and differential.
Genevestigatori P99024.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype."
    Wang D., Villasante A., Lewis S.A., Cowan N.J.
    J. Cell Biol. 103:1903-1910(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Bone marrow, Embryo, Kidney, Liver, Pituitary, Placenta, Spinal ganglion, Spleen, Sympathetic ganglion and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 3-19; 63-121; 163-174; 217-241; 242-276; 283-297; 310-318; 321-359 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  6. "Five mouse tubulin isotypes and their regulated expression during development."
    Lewis S.A., Lee M.G.-S., Cowan N.J.
    J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 325-444.
  7. Cited for: POLYGLUTAMYLATION.
  8. "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
    Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
    J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP10.
  9. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYGLYCYLATION.
  10. Cited for: INTERACTION WITH PIFO.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiTBB5_MOUSE
AccessioniPrimary (citable) accession number: P99024
Secondary accession number(s): B1B178
, P05218, Q3TFB6, Q3THH9, Q3TIL1, Q3UAV4, Q3UF52, Q8WUC1, Q9CY33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3